Anti-Prion protein PrP Antibody (RMAB-0250995)
Cat. No.: RMAB-0250995
Category: Primary Antibodies
INQUIRY
50 μL
Customer Size
Mouse monoclonal to Prion protein PrP
Product Features
| Isotype | IgG2b |
|---|---|
| Clonality | Monoclonal |
| Host Species | Mouse |
| Clone Number | 8H4 |
| Form | Liquid |
| Purity | IgG fraction |
| Species Reactivity | Mouse, Rat, Sheep, Cow, Human, Monkey |
| Immunogen | Recombinant full length protein corresponding to Mouse Prion protein PrP. |
| Applications | IP, Indirect ELISA, WB, ICC, IHC-P, Flow Cyt |
| Key Features | Mouse monoclonal to Prion protein PrP; Suitable for: IP, Indirect ELISA, WB, ICC, IHC-P, Flow Cyt; Reacts with: Mouse, Rat, Sheep, Cow, Human, Monkey; Isotype: IgG2b |
Target Information
| Target Symbol | PRNP |
|---|---|
| Target Name | Alternative prion protein |
| UniProt ID | P04156 |
| Cellular Localization | Cell membrane. Golgi apparatus and Cytoplasm. Nucleus. Accumulates outside the secretory route in the cytoplasm, from where it relocates to the nucleus. |
| Epitope | The antibody epitope resides within amino acids 145-180 of human Prion protein PrP. |
| Function | The function of PrP is still under debate. May play a role in neuronal development and synaptic plasticity. May be required for neuronal myelin sheath maintenance. May play a role in iron uptake and iron homeostasis (By similarity). Isoform 2 may act as a growth suppressor by arresting the cell cycle at the G/G1 phase. Soluble oligomers are toxic to cultured neuroblastoma cells and induce apoptosis (in vitro). |
| Involvement in Disease | PrP is found in high quantity in the brain of humans and animals infected with neurodegenerative diseases known as transmissible spongiform encephalopathies or prion diseases, like: Creutzfeldt-Jakob disease (CJD), fatal familial insomnia (FFI), Gerstmann-Straussler disease (GSD), Huntington disease-like type 1 (HDL1) and kuru in humans; scrapie in sheep and goat; bovine spongiform encephalopathy (BSE) in cattle; transmissible mink encephalopathy (TME); chronic wasting disease (CWD) of mule deer and elk; feline spongiform encephalopathy (FSE) in cats and exotic ungulate encephalopathy (EUE) in nyala and greater kudu. The prion diseases illustrate three manifestations of CNS degeneration: (1) infectious (2) sporadic and (3) dominantly inherited forms. TME, CWD, BSE, FSE, EUE are all thought to occur after consumption of prion-infected foodstuffs.Defects in PRNP are the cause of Creutzfeldt-Jakob disease (CJD). CJD occurs primarily as a sporadic disorder (1 per million), while 1-15% are familial. Accidental transmission of CJD to humans appears to be iatrogenic (contaminated human growth hormone (HGH), corneal transplantation, electroencephalographic electrode implantation, etc.). Epidemiologic studies have failed to implicate the ingestion of infected annimal meat in the pathogenesis of CJD in human. The triad of microscopic features that characterize the prion diseases consists of (1) spongiform degeneration of neurons, (2) severe astrocytic gliosis that often appears to be out of proportion to the degree of nerve cell loss, and (3) amyloid plaque formation. CJD is characterized by progressive dementia and myoclonic seizures, affecting adults in mid-life. Some patients present sleep disorders, abnormalities of high cortical function, cerebellar and corticospinal disturbances. The disease ends in death after a 3-12 months illness.Defects in PRNP are the cause of fatal familial insomnia (FFI). FFI is an autosomal dominant disorder and is characterized by neuronal degeneration limited to selected thalamic nuclei and progressive insomnia.Defects in PRNP are the cause of Gerstmann-Straussler disease (GSD). GSD is a heterogeneous disorder and was defined as a spinocerebellar ataxia with dementia and plaquelike deposits. GSD incidence is less than 2 per 1 million live births.Defects in PRNP are the cause of Huntington disease-like type 1 (HDL1). HDL1 is an autosomal dominant, early onset neurodegenerative disorder with prominent psychiatric features.Defects in PRNP are the cause of kuru (KURU). Kuru is transmitted during ritualistic cannibalism, among natives of the New Guinea highlands. Patients exhibit various movement disorders like cerebellar abnormalities, rigidity of the limbs, and clonus. Emotional lability is present, and dementia is conspicuously absent. Death usually occurs from 3 to 12 month after onset.Defects in PRNP are the cause of spongiform encephalopathy with neuropsychiatric features (SENF); an autosomal dominant presenile dementia with a rapidly progressive and protracted clinical course. The dementia was characterized clinically by frontotemporal features, including early personality changes. Some patients had memory loss, several showed aggressiveness, hyperorality and verbal stereotypy, others had parkinsonian symptoms. |
| Post-translational Modifications | The glycosylation pattern (the amount of mono-, di- and non-glycosylated forms or glycoforms) seems to differ in normal and CJD prion. Isoform 2 is sumoylated by SUMO1. |
| Myeloma | Sp2/ |
| Domain | The normal, monomeric form has a mainly alpha-helical structure. The disease-associated, protease-resistant form forms amyloid fibrils containing a cross-beta spine, formed by a steric zipper of superposed beta-strands. Disease mutations may favor intermolecular contacts via short beta strands, and may thereby trigger oligomerization. Contains an N-terminal region composed of octamer repeats. At low copper concentrations, the sidechains of His residues from three or four repeats contribute to the binding of a single copper ion. Alternatively, a copper ion can be bound by interaction with the sidechain and backbone amide nitrogen of a single His residue. The observed copper binding stoichiometry suggests that two repeat regions cooperate to stabilize the binding of a single copper ion. At higher copper concentrations, each octamer can bind one copper ion by interactions with the His sidechain and Gly backbone atoms. A mixture of binding types may occur, especially in the case of octamer repeat expansion. Copper binding may stabilize the conformation of this region and may promote oligomerization. |
| Sequence Similarities | Belongs to the prion family. |
Storage & Shipping
| Storage Buffer | pH: 7.40; Preservative: 0.097% Sodium azide; Constituent: 0.0268% PBS |
|---|---|
| Storage & Shipping | Shipped at 4°C. Upon delivery aliquot and store at -20°C or -80°C. Avoid repeated freeze / thaw cycles. |
For research use only. Not for clinical use.
